ID SNL1_ARATH Reviewed; 1372 AA. AC Q9SRH9; DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 27-MAR-2024, entry version 123. DE RecName: Full=Paired amphipathic helix protein Sin3-like 1; GN Name=SNL1; OrderedLocusNames=At3g01320; ORFNames=T22N4.5; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION RP WITH ALY2; ALY3; GATA21; TBP1; TRP2; TKI1; VAL1; SKP1B; FBX5 AND PUB14, RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=19962994; DOI=10.1016/j.jmb.2009.11.065; RA Bowen A.J., Gonzalez D., Mullins J.G., Bhatt A.M., Martinez A., RA Conlan R.S.; RT "PAH-domain-specific interactions of the Arabidopsis transcription RT coregulator SIN3-LIKE1 (SNL1) with telomere-binding protein 1 and ALWAYS RT EARLY2 Myb-DNA binding factors."; RL J. Mol. Biol. 395:937-949(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."; RL Nature 408:820-822(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). CC -!- FUNCTION: Acts as a transcriptional repressor. An histone deacetylase CC (HDAC) activity is required for transcription repression. May play a CC role in telomere stability. {ECO:0000269|PubMed:19962994}. CC -!- SUBUNIT: Interacts (via PAH3) with ALY2. Interacts (via PAH2) with CC TBP1. Interacts with ALY3, GATA21, TRP2, TKI1, VAL1, SKP1B, FBX5 and CC PUB14. {ECO:0000269|PubMed:19962994}. CC -!- INTERACTION: CC Q9SRH9; Q6A333: ALY2; NbExp=2; IntAct=EBI-2616294, EBI-2616358; CC Q9SRH9; Q9FFY9: TRP4; NbExp=2; IntAct=EBI-2616294, EBI-2616485; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810, CC ECO:0000269|PubMed:19962994}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=Q9SRH9-1; Sequence=Displayed; CC -!- SEQUENCE CAUTION: CC Sequence=AAF03494.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC010676; AAF03494.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002686; AEE73639.1; -; Genomic_DNA. DR RefSeq; NP_186781.4; NM_110998.5. [Q9SRH9-1] DR AlphaFoldDB; Q9SRH9; -. DR SMR; Q9SRH9; -. DR BioGRID; 6598; 14. DR IntAct; Q9SRH9; 13. DR STRING; 3702.Q9SRH9; -. DR iPTMnet; Q9SRH9; -. DR PaxDb; 3702-AT3G01320-1; -. DR ProteomicsDB; 232626; -. [Q9SRH9-1] DR EnsemblPlants; AT3G01320.1; AT3G01320.1; AT3G01320. [Q9SRH9-1] DR GeneID; 821265; -. DR Gramene; AT3G01320.1; AT3G01320.1; AT3G01320. [Q9SRH9-1] DR KEGG; ath:AT3G01320; -. DR Araport; AT3G01320; -. DR TAIR; AT3G01320; SNL1. DR eggNOG; KOG4204; Eukaryota. DR InParanoid; Q9SRH9; -. DR OMA; NYFKSFD; -. DR OrthoDB; 199155at2759; -. DR PRO; PR:Q9SRH9; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9SRH9; baseline and differential. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR Gene3D; 1.20.1160.11; Paired amphipathic helix; 3. DR InterPro; IPR013194; HDAC_interact_dom. DR InterPro; IPR003822; PAH. DR InterPro; IPR036600; PAH_sf. DR InterPro; IPR039774; Sin3-like. DR InterPro; IPR031693; Sin3_C. DR PANTHER; PTHR12346:SF67; PAIRED AMPHIPATHIC HELIX PROTEIN SIN3-LIKE 1; 1. DR PANTHER; PTHR12346; SIN3B-RELATED; 1. DR Pfam; PF02671; PAH; 3. DR Pfam; PF08295; Sin3_corepress; 1. DR Pfam; PF16879; Sin3a_C; 1. DR SMART; SM00761; HDAC_interact; 1. DR SUPFAM; SSF47762; PAH2 domain; 3. DR PROSITE; PS51477; PAH; 3. DR Genevisible; Q9SRH9; AT. PE 1: Evidence at protein level; KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Repressor; Transcription; Transcription regulation. FT CHAIN 1..1372 FT /note="Paired amphipathic helix protein Sin3-like 1" FT /id="PRO_0000394040" FT DOMAIN 51..121 FT /note="PAH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810" FT DOMAIN 136..206 FT /note="PAH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810" FT DOMAIN 331..400 FT /note="PAH 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810" FT REGION 1..50 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 210..244 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 272..323 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 764..783 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 791..817 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 934..1056 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 15..32 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 210..228 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 272..314 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 794..808 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 941..964 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 971..992 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 993..1014 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1039..1056 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1049 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9LFQ3" SQ SEQUENCE 1372 AA; 156209 MW; 60E5F3E09F38B0C0 CRC64; MKRIRDDVYA SGSQFRRPLG SSRGQLCGQS PVHGSGDTEE EEEGGSRRVS QKLTTNDALS YLREVKEMFQ DQREKYDRFL EVMKDFKAQR TDTGGVIARV KELFKGHNNL IYGFNTFLPK GYEITLIEED DALPKKTVEF EQAINFVNKI KMRFKHDEHV YKSFLEILNM YRKENKEIKE VYNEVSILFQ GHLDLLEQFT RFLPASLPSH SAAQHSRSQA QQYSDRGSDP PLLHQMQVEK ERRRERAVAL RGDYSVERYD LNDDKTMVKI QREQRKRLDK ENRARRGRDL DDREAGQDNL HHFPEKRKSS RRAEALEAYS GSASHSEKDN LKSMYKQAFV FCEKVKDRLC SQDDYQTFLK CLNIFSNGII QRKDLQNLVS DLLGKFPDLM DEFNQFFERC ESITDGFQRL AGVMSKKLFS SEEQLSRPMK VEEKESEHKP ELEAVKETEQ CKKEYMGKSI QELDLSDCEC CTPSYRLLPA DYPIPIASQR SELGAEVLND HWVSVTSGSE DYSFKHMRRN QYEESLFRCE DDRFELDMLL ESVSSAARSA ESLLNIITEK KISFSGSFRI EDHFTALNLR CIERLYGDHG LDVIDILNKN PATALPVILT RLKQKQGEWK KCRDDFDKVW ANVYAKNHYK SLDHRSFYFK QQDSKNLSAK SLLAEIKELK EKSQNDDDVL LSISAGYRQP INPNLEYEYL NRAIHEDMFK VVQFSCEELC STKEQLSKVL RLWENFLEAV LGVPPRAKGT DLVEDVVINP KTLDVNHSTS PNGEAAVSSG GDTARLASRK LKSAANGDEN SSSGTFKHGI GLLNKDSTGK ENLEDVEIAN RDGVACSAVK PQKEQETGNE AEKRFGKPIP MDISERAAIS SISIPSGAEN NHCVVGKEVL PGAHEIQAKP SDTLTDIHHD VDSIETVHST QGGDVGNSIV LANGLRSDSS KGTRNSDDPE GPSRNEKEEG ELSPNGDFED NFGVYKDHGV KSTSKPENSA EAEVEADAEV ENEDDADDVD SENASEASGT ESGGDVCSQD EDREEENGEH DEIDGKAESE GEAEGMDPHL LEGESELLPQ SERVLLSVRP LSKHVAAVLC DERTKDLQVF YGNDDFYVLF RLHQILYERI LYAKRNCSGG ELKSKNLKDT NAGDPYARFM RVLYGLLDGS AENTKFEDEC RAIIGNQSYV LFTLDKLIYR LVKQLQAIVA DEMDNKLLQL YEYEKSRKPG RVIDSVYYEN VRVLVHEENI YRLECSSLPS RLSIQLMDNI IEKPEAYAVS MDPTFASYMQ TELLSVSSGK KEEGHDIVLQ RNLTGLYDLC KAMEGVEVVN GLECKMSCSS YKIAYVLDTE DYFHRKKKKK KTEQLWQRNK VRVERFHRFL SA //